As the specificity of a ribozyme is commonly defined as its ability to discriminate between similar substrates [1], a collection of five substrates possessing identical ribozyme binding domains, but different biosensor sequences, was synthesized (Figure 1D).
Previously reported analyses of HDV ribozyme cleavage using a collection of small substrates revealed that the identity of the base pairs involving the pairing of substrate position +4 with the ribozyme significantly influenced the activity level [47].
It was also shown that when the MLC approach is compared to a single label classification, it coherently reflects the actual metabolism information when applied over a collection of CYP450 substrates [30].
Previously, a collection of small substrates possessing both single and multiple mutations in positions −1 to −4 was studied [49].
Based on these results, we decided to investigate the labeling of SNAPf with a collection of fluorogenic substrates containing combinations of fluorophore/quencher pairs spanning the visible spectrum.
To study this "translocase" (helicase) activity, we have designed a collection of Rho substrate chimeras containing an RNA DNA helix located at various positions with respect to a short (47 nucleotides) artificial loading site.
We challenged the ability of the crude termite extract to degrade a wide collection of substrates, including natural polysaccharides and pNP derivatives.
We focused this work on natural and synthetic CYP1A enzymes and a collection of 16 steroidal substrates, 14 steroids, and 2 steroid analogues, a terpenoid and a drug.
The collection of substrates includes proteins involved in multiple cellular processes including cell-cell adhesion, endocytosis, and signal transduction.
The selected collection of substrates differ widely with regard to fundamental properties, such as crystallinity, degree of polymerization (DP), and complexity (Table 2).
The results from this study accordingly present a collection of candidates to search for PDZ-interacting substrates in border cells and other migratory cells.
